Reif U, Winterhoff U, Doerfler W
Eur J Biochem. 1977 Mar 1;73(2):327-33. doi: 10.1111/j.1432-1033.1977.tb11322.x.
The properties of the pH 4.0 endonuclease from adenovirus-type-2-infected KB cells were determined. The enzyme has a molecular weight of approximately 40000. Its pH optimum is at pH 4.0, it is not inhibited by ethylenediaminetetraacetate (EDTA), and it is active at temperatures up to 60 degree C. The enzyme cleaves adenovirus DNA in a stepwise manner. The limit digestion product has a molecular weight of 120000-200000. There is evidence that the cleavage reaction proceeds via an initial single-strand nick. Under the conditions tested the endonuclease did not seem to reveal a high degree of specificity as to the recognition of cleavage sites, or else the sites recognized occurred very frequently.
测定了来自2型腺病毒感染的KB细胞的pH 4.0核酸内切酶的特性。该酶的分子量约为40000。其最适pH为4.0,不受乙二胺四乙酸(EDTA)抑制,在高达60℃的温度下仍有活性。该酶以逐步方式切割腺病毒DNA。极限消化产物的分子量为120000 - 200000。有证据表明切割反应通过最初的单链切口进行。在所测试的条件下,核酸内切酶似乎对切割位点的识别没有高度特异性,否则所识别的位点非常频繁地出现。